ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity

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dc.contributor.author Anéas, M.a.f.
dc.contributor.author Portaro, Fernanda Calheta Vieira [UNIFESP]
dc.contributor.author Lebrun, Ivo
dc.contributor.author Juliano, Luiz [UNIFESP]
dc.contributor.author Palma, M.s.
dc.contributor.author Fernandes, B.l.
dc.date.accessioned 2015-06-14T13:29:31Z
dc.date.available 2015-06-14T13:29:31Z
dc.date.issued 2001-11-01
dc.identifier http://dx.doi.org/10.1590/S0100-879X2001001100004
dc.identifier.citation Brazilian Journal of Medical and Biological Research. Associação Brasileira de Divulgação Científica, v. 34, n. 11, p. 1397-1403, 2001.
dc.identifier.issn 0100-879X
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/1268
dc.description.abstract The opportunistic bacterium Proteus mirabilis secretes a metalloprotease, ZapA, considered to be one of its virulence factors due to its IgA-degrading activity. However, the substrate specificity of this enzyme has not yet been fully characterized. In the present study we used fluorescent peptides derived from bioactive peptides and the oxidized ß-chain of insulin to determine the enzyme specificity. The bradykinin- and dynorphin-derived peptides were cleaved at the single bonds Phe-Ser and Phe-Leu, with catalytic efficiencies of 291 and 13 mM/s, respectively. Besides confirming already published cleavage sites, a novel cleavage site was determined for the ß-chain of insulin (Val-Asn). Both the natural and the recombinant enzyme displayed the same broad specificity, demonstrated by the presence of hydrophobic, hydrophilic, charged and uncharged amino acid residues at the scissile bonds. Native IgA, however, was resistant to hydrolysis by ZapA. en
dc.format.extent 1397-1403
dc.language.iso eng
dc.publisher Associação Brasileira de Divulgação Científica
dc.relation.ispartof Brazilian Journal of Medical and Biological Research
dc.rights Acesso aberto
dc.subject Proteus mirabilis en
dc.subject metalloprotease en
dc.subject substrate specificity en
dc.subject fluorogenic peptides en
dc.subject IgA en
dc.subject insulin ß-chain en
dc.title ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity en
dc.type Artigo
dc.contributor.institution Universidade de São Paulo (USP)
dc.contributor.institution Instituto Butantan CEPID-FAPESP Centro de Toxinologia Aplicada
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution Universidade Estadual Paulista (UNESP)
dc.description.affiliation Universidade de São Paulo Instituto de Ciências Biomédicas Departamento de Microbiologia
dc.description.affiliation Instituto Butantan CEPID-FAPESP Centro de Toxinologia Aplicada
dc.description.affiliation Universidade Federal de São Paulo (UNIFESP) CEPID-FAPESP Centro de Toxinologia Aplicada
dc.description.affiliation Universidade Estadual Paulista CEPID-FAPESP Centro de Toxinologia Aplicada
dc.description.affiliationUnifesp UNIFESP, CEPID-FAPESP Centro de Toxinologia Aplicada
dc.identifier.file S0100-879X2001001100004.pdf
dc.identifier.scielo S0100-879X2001001100004
dc.identifier.doi 10.1590/S0100-879X2001001100004
dc.description.source SciELO
dc.identifier.wos WOS:000172765400004



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